1F1Z

TNSA, a catalytic component of the TN7 transposition system

Summary for 1F1Z

• Entry DOI: 10.2210/pdb1f1z/pdb
• Descriptor: TNSA ENDONUCLEASE, MAGNESIUM ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: restriction endonuclease fold, dna binding protein
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 62761.52

Authors

Hickman, A.B.,Li, Y.,Mathew, S.V.,May, E.W.,Craig, N.L.,Dyda, F. (deposition date: 2000-05-21, release date: 2000-06-28, Last modification date: 2024-02-07)

Primary citation

Hickman, A.B.,Li, Y.,Mathew, S.V.,May, E.W.,Craig, N.L.,Dyda, F.
Unexpected structural diversity in DNA recombination: the restriction endonuclease connection.
Mol.Cell, 5:1025-1034, 2000

PubMed Abstract: Transposition requires a coordinated series of DNA breakage and joining reactions. The Tn7 transposase contains two proteins: TnsA, which carries out DNA breakage at the 5' ends of the transposon, and TnsB, which carries out breakage and joining at the 3' ends of the transposon. TnsB is a member of the retroviral integrase superfamily whose hallmark is a conserved DDE motif. We report here the structure of TnsA at 2.4 A resolution. Surprisingly, the TnsA fold is that of a type II restriction endonuclease. Thus, Tn7 transposition involves a collaboration between polypeptides, one containing a DDE motif and one that does not. This result indicates that the range of biological processes that utilize restriction enzyme-like folds also includes DNA transposition.

PubMed: 10911996
DOI: 10.1016/S1097-2765(00)80267-1

Experimental method

X-RAY DIFFRACTION (2.4 Å)